Formation and Cooperative Behaviour of Protein Complexes on the Cell Membrane
Seiten
2013
Springer Berlin (Verlag)
978-3-642-26994-3 (ISBN)
Springer Berlin (Verlag)
978-3-642-26994-3 (ISBN)
Framed by a statistical physics perspective, this volume describes both the process of self-assembly and the impact of spatial organization on the function of membrane proteins. Using methods from equilibrium and non-equilibrium statistical mechanics, the text demonstrates the importance of the protein-protein interactions.
With the aim of providing a deeper insight into possible mechanisms of biological self-organization, this thesis presents new approaches to describe the process of self-assembly and the impact of spatial organization on the function of membrane proteins, from a statistical physics point of view. It focuses on three important scenarios: the assembly of membrane proteins, the collective response of mechanosensitive channels and the function of the twin arginine translocation (Tat) system. Using methods from equilibrium and non-equilibrium statistical mechanics, general conclusions were drawn that demonstrate the importance of the protein-protein interactions. Namely, in the first part a general aggregation dynamics model is formulated, and used to show that fragmentation crucially affects the efficiency of the self-assembly process of proteins. In the second part, by mapping the membrane-mediated forces into a simplified many-body system, the dynamic and equilibrium behaviour of interacting mechanosensitive channels is derived, showing that protein agglomeration strongly impacts its desired function. The final part develops a model that incorporates both the agglomeration and transport function of the Tat system, thereby providing a comprehensive description of this self-organizing process.
With the aim of providing a deeper insight into possible mechanisms of biological self-organization, this thesis presents new approaches to describe the process of self-assembly and the impact of spatial organization on the function of membrane proteins, from a statistical physics point of view. It focuses on three important scenarios: the assembly of membrane proteins, the collective response of mechanosensitive channels and the function of the twin arginine translocation (Tat) system. Using methods from equilibrium and non-equilibrium statistical mechanics, general conclusions were drawn that demonstrate the importance of the protein-protein interactions. Namely, in the first part a general aggregation dynamics model is formulated, and used to show that fragmentation crucially affects the efficiency of the self-assembly process of proteins. In the second part, by mapping the membrane-mediated forces into a simplified many-body system, the dynamic and equilibrium behaviour of interacting mechanosensitive channels is derived, showing that protein agglomeration strongly impacts its desired function. The final part develops a model that incorporates both the agglomeration and transport function of the Tat system, thereby providing a comprehensive description of this self-organizing process.
Introduction.- The Role of Fragmentation on the Formation of Homomeric Protein Complexes.- Collective Response of Self-organised Clusters of Mechanosensitive Channels.- Assembly and Fragmentation of Tat Pores.- Conclusion.
| Erscheint lt. Verlag | 29.11.2013 |
|---|---|
| Reihe/Serie | Springer Theses |
| Zusatzinfo | XII, 80 p. |
| Verlagsort | Berlin |
| Sprache | englisch |
| Maße | 155 x 235 mm |
| Gewicht | 156 g |
| Themenwelt | Naturwissenschaften ► Biologie ► Mikrobiologie / Immunologie |
| Naturwissenschaften ► Physik / Astronomie ► Angewandte Physik | |
| Schlagworte | macromolecular dynamics • Mechanosensitive channels • Membrane functional organization • Outstanding PhD Thesis • Protein assembly • protein-protein interactions • Self-organization and self-assembly |
| ISBN-10 | 3-642-26994-X / 364226994X |
| ISBN-13 | 978-3-642-26994-3 / 9783642269943 |
| Zustand | Neuware |
| Informationen gemäß Produktsicherheitsverordnung (GPSR) | |
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